Characterization and comparison of aminopeptidase activity of various strains of Mycobacterium tuberculosis.
The aminopeptidase activity of three strains of Mycobacterium tuberculosis, H37Rv, H37Ra, and M. tuberculosis from a patient, was partially purified and characterized. The activity from all three organisms was found to be very similar, if not identical. All three aminopeptidases eluted at a similar salt concentration on DEAE Bio-Gel; were active on the same synthetic and peptide substrates; had molecular weights of 75-76,000; were found to be stable between pH 5 and 8, and 4 degrees and 40 degrees C; and had a pH optimum of 7. They were inhibited by low concentrations of Hg2+, Cu2+ and Co2+; metal chelators; and 4-chloromercuribenzoic acid. A number of amino acids and several antibiotics were also found to be inhibitory. Of the antibiotics tested, rifampicin and bacitracin were the most effective.
D000626:Aminopeptidases / Q000032:analysis* / Q000037:antagonists & inhibitors; D001414:Bacitracin / Q000494:pharmacology; D002850:Chromatography, Gel; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D009169:Mycobacterium tuberculosis / Q000201:enzymology*; D013379:Substrate Specificity
D001414:Bacitracin; D000626:Aminopeptidases